Summary: Glycosyl hydrolase 108
This is the Wikipedia entry entitled "Glycoside hydrolase family 108". More...
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Glycoside hydrolase family 108 Edit Wikipedia article
|Glycosyl hydrolase 108|
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 108 CAZY GH_108 includes enzymes with lysozyme (N-acetylmuramidase) EC 22.214.171.124 activity. A glutamic acid residue within a conserved Glu-Gly-Gly-Tyr motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion.
- Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- Stojković EA, Rothman-Denes LB (2007). "Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases.". J Mol Biol 366 (2): 406–19. doi:10.1016/j.jmb.2006.11.028. PMID 17174325.
- Pei J, Grishin NV (2005). "COG3926 and COG5526: a tale of two new lysozyme-like protein families.". Protein Sci 14 (10): 2574–81. doi:10.1110/ps.051656805. PMC 2253296. PMID 16155206.
- Kondo Y, Toyoda A, Fukushi H, Yanase H, Tonomura K, Kawasaki H et al. (1994). "Cloning and characterization of a pair of genes that stimulate the production and secretion of Zymomonas mobilis extracellular levansucrase and invertase.". Biosci Biotechnol Biochem 58 (3): 526–30. PMID 7764692.
Glycosyl hydrolase 108 Provide feedback
This family acts as a lysozyme (N-acetylmuramidase), EC:126.96.36.199. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity . In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion [2,3]. It is frequently found at the N-terminus of proteins containing a C-terminal PF09374 domain.
Kondo Y, Toyoda A, Fukushi H, Yanase H, Tonomura K, Kawasaki H, Sakai T;, Biosci Biotechnol Biochem. 1994;58:526-530.: Cloning and characterization of a pair of genes that stimulate the production and secretion of Zymomonas mobilis extracellular levansucrase and invertase. PUBMED:7764692 EPMC:7764692
External database links
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Barley chitinase, bacterial chitosanase, and lysozymes from phage and animals all hydrolyse related polysaccharides. The proteins little amino-acid similarity, but have a structurally invariant core consisting of two helices and a three-stranded beta-sheet which form the substrate-binding and catalytic cleft .
The clan contains the following 12 members:Glucosaminidase Glyco_hydro_108 Glyco_hydro_19 Glyco_hydro_46 Lys Lysozyme_like Phage_lysozyme REGB_T4 SLT SLT_2 TraH_2 Transglycosylas
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Curation and family details
|Seed source:||Pfam-B_8737 (release 8.0)|
|Author:||Moxon SJ, Bateman A, Eberhardt R|
|Number in seed:||20|
|Number in full:||820|
|Average length of the domain:||85.40 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||42.35 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Glyco_hydro_108 domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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